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Titolo:
Lectin-induced inhibition of desensitization of the kainate receptor GluR6depends on the activation state and can be mediated by a single native or ectopic N-linked carbohydrate side chain
Autore:
Everts, I; Petroski, R; Kizelsztein, P; Teichberg, VI; Heinemann, SF; Hollmann, M;
Indirizzi:
MaxyPlanck Inst Expt Med, Glutamate Receptor Lab, D-37075 Gottingen, German Max Planck Inst Expt Med Gottingen Germany D-37075 075 Gottingen, German Salk Inst Biol Studies, Mol Neurobiol Lab, La Jolla, CA 92037 USA Salk Inst Biol Studies La Jolla CA USA 92037 Lab, La Jolla, CA 92037 USA Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 biol, IL-76100 Rehovot, Israel
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 3, volume: 19, anno: 1999,
pagine: 916 - 927
SICI:
0270-6474(19990201)19:3<916:LIODOT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMATE-RECEPTOR; CONCANAVALIN-A; BINDING-PROTEINS; AMPA RECEPTORS; ACID RECEPTORS; MODULATION; GLYCOSYLATION; CYCLOTHIAZIDE; QUISQUALATE; NEURONS;
Keywords:
GluR6; kainate receptor; N-glycosylation; lectin; concanavalin A; receptor desensitization; ectopic sites; mutagenesis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Hollmann, M Max75lanck Inst Expt Med, Glutamate Receptor Lab, Hermann ReinStr 3, D-370 Max Planck Inst Expt Med Hermann Rein Str 3 Gottingen Germany D-37075
Citazione:
I. Everts et al., "Lectin-induced inhibition of desensitization of the kainate receptor GluR6depends on the activation state and can be mediated by a single native or ectopic N-linked carbohydrate side chain", J NEUROSC, 19(3), 1999, pp. 916-927

Abstract

The ionotropic glutamate receptor GluR6 exhibits strongly and rapidly desensitizing current responses. Treatment of heterologically expressed GluR6 with the lectin concanavalin A (ConA) in Xenopus oocytes as well as in humanembryonic kidney-293 cells results in a considerable increase of the steady-state current, presumably by inhibiting receptor desensitization. In the present study, we investigated the molecular basis of this effect using a systematic mutagenesis approach. We found that although N-glycosylation is an absolute prerequisite for the tectin-mediated inhibition of desensitization, no single one of the nine extracellular consensus sites for N-glycosylation of GluR6 is required. Rather, each of the nine N-linked carbohydrate side chains is independently capable of modulatory interaction with the lectin. Moreover, even artificially introduced N-glycosylation sites can substitute for native sites. Thus, the specific site of the lectin binding does not appear to be important for its desensitization-inhibiting action. Furthermore, we show that the extent of the receptor's ConA sensitivity depends on its state of activation, because the desensitized GluR6 exhibits significantly lower lectin sensitivity than the nondesensitized receptor. We conclude that binding of ConA "locks" the receptor in the activatable state, thereby inhibiting conformational changes required to shift the receptor to thedesensitized state.

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Documento generato il 09/07/20 alle ore 01:19:40